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Cloning, recombinant expression and biochemical characterization of the murine CD83 molecule which is specifically upregulated during dendritic cell maturation
Author(s) -
Berchtold Susanne,
Mühl-Zürbes Petra,
Heufler Christine,
Winklehner Patrizia,
Schuler Gerold,
Steinkasserer Alexander
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01465-9
Subject(s) - complementary dna , microbiology and biotechnology , amino acid , molecular cloning , recombinant dna , signal peptide , transfection , biology , downregulation and upregulation , expression cloning , cloning (programming) , peptide sequence , messenger rna , chemistry , biochemistry , gene , computer science , programming language
Human CD83 (hCD83) is a glycoprotein expressed predominantly on the surface of dendritic cells (DC) and represents the best marker for mature DC. Here, we report the cloning of the cDNA encoding mouse CD83 (mCD83) from a murine bone marrow‐derived DC (BM‐DC) cDNA library. DNA sequence analysis revealed a 196 amino acid protein including a signal peptide of 21 amino acids which shares 63% amino acid identity with hCD83. Using Northern blot analyses, mCD83 mRNA was found to be strongly expressed in mouse BM‐DC and its expression was upregulated following stimulation with LPS or TNF‐α. Transfection experiments using COS‐7 cells revealed that mCD83 is glycosylated. Furthermore, the extracellular CD83 domain was recombinantly expressed in Escherichia coli and one‐dimensional NMR data strongly support that the protein is structurally folded.